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Cryoem reconstruction of human IKK1, closed conformation 3

Analyse Cryoem reconstruction of human IKK1, closed conformation 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TQY
Type: protein
Length: 1,156 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inhibitor of nuclear factor kappa-B kinase subunit alpha
EC: 2.7.11.10
UniProt: O15111
Pockets: 16 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 58% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Inhibitor of nuclear factor kappa-B kinase subunit alpha (EC 2.7.11.10)	protein	578	58% helix, 11% strand	O15111

Pockets

16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.76	0.97	19	empty
2	71	0.73	0.97	18	empty
3	513	0.70	0.80	45	empty
4	518	0.69	0.79	48	empty
5	591	0.68	0.78	52	empty

Interfaces

1 interface between chains.

A–B · 1455 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5TQY · CryoEM reconstruction of human IKK1, closed conformation 3 · the same entry in another collection · chain A against A, TM-score 1.00
O15111 · AlphaFold monomer V2.0 prediction for inhibitor of nuclear factor kappa-B kinase subunit… · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O15111
Elsewhere: RCSB PDB 5TQY · PDBe 5TQY · UniProt O15111

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